3A24
Crystal structure of BT1871 retaining glycosidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 122.962, 167.100, 192.182 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.940 - 2.300 |
| R-factor | 0.186 |
| Rwork | 0.186 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2d73 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Number of reflections | 87930 | |
| Completeness [%] | 100.0 | 99.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 293 | 100mM MES/NaOH buffer, 12% PEG 6000, 10% PEG 10000, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
